6VOA
Cryo-EM structure of the BBSome-ARL6 complex
Summary for 6VOA
| Entry DOI | 10.2210/pdb6voa/pdb |
| EMDB information | 21259 |
| Descriptor | Bardet-Biedl syndrome 18 protein, Bardet-Biedl syndrome 2 protein homolog, Bardet-Biedl syndrome 4 protein homolog, ... (9 entities in total) |
| Functional Keywords | cilia, bardet-biedl syndrome, protein transport |
| Biological source | Bos taurus (Bovine) More |
| Total number of polymer chains | 9 |
| Total formula weight | 507566.42 |
| Authors | Yang, S.,Walz, T.,Nachury, M.V. (deposition date: 2020-01-30, release date: 2020-06-24, Last modification date: 2024-03-06) |
| Primary citation | Yang, S.,Bahl, K.,Chou, H.T.,Woodsmith, J.,Stelzl, U.,Walz, T.,Nachury, M.V. Near-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes. Elife, 9:-, 2020 Cited by PubMed Abstract: Dynamic trafficking of G protein-coupled receptors (GPCRs) out of cilia is mediated by the BBSome. In concert with its membrane recruitment factor, the small GTPase ARL6/BBS3, the BBSome ferries GPCRs across the transition zone, a diffusion barrier at the base of cilia. Here, we present the near-atomic structures of the BBSome by itself and in complex with ARL6, and we describe the changes in BBSome conformation induced by ARL6 binding. Modeling the interactions of the BBSome with membranes and the GPCR Smoothened (SMO) reveals that SMO, and likely also other GPCR cargoes, must release their amphipathic helix 8 from the membrane to be recognized by the BBSome. PubMed: 32510327DOI: 10.7554/eLife.55954 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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